New generations of therapeutic proteins and antibodies are being engineered and developed that have a host of performance improvements, including modified affinities, increased stability, reduced or increased cross-reactivity, greater solubility, and the like, e.g. Igawa et al, mAbs. 3(3): 243-252 (2011); Bostrom et al, Science, 323: 1610-1614 (2009). An important approach for making such improvements is to create a mutant library from an existing therapeutic protein or therapeutic candidate, then screen library members by various assays until better performing proteins are found. Because such libraries are typically very large, such screening can be expensive and time consuming unless high throughput tools are available. In particular, the target specificity and non-specific binding properties of candidate compounds have been difficult to assess efficiently because of a dearth of high-throughput techniques for this purpose.
In view of the above, endeavors that require an understanding of protein binding reactions, such as protein and antibody engineering, would be advanced by the availability of efficient techniques for creating representative low complexity libraries from which properties of candidate binding compounds could be rapidly assessed/selected.